ArticleThe Journal of cell biology1991
Neonatal and adult myosin heavy chains form homodimers during avian skeletal muscle development.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Myosin V: regulation by calcium, calmodulin, and the tail domain.The Journal of cell biology · 2004Article
- Does the myosin V neck region act as a lever?Journal of muscle research and cell motility · 2004Article
- A mutant heterodimeric myosin with one inactive head generates maximal displacement.The Journal of cell biology · 2003Article
- The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.The Journal of cell biology · 2002Article
- Evidence for differential post-translational modifications of slow myosin heavy chain during murine skeletal muscle development.Journal of muscle research and cell motility · 2000Article
- Development and composition of skeletal muscle fibres in mouse oesophagus.Journal of muscle research and cell motility · 2000Article
- Developmental transitions in the myosin patterns of two fast muscles.Journal of muscle research and cell motility · 1993Article
- Distribution of developmental myosin isoforms in isolated A-segments.Journal of muscle research and cell motility · 1992Article
- Assembly of avian skeletal muscle myosins: evidence that homodimers of the heavy chain subunit are the thermodynamically stable form.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Myosin isoforms contribute to the heterogeneity and adaptability of skeletal muscle fibers. Besides the well-characterized slow and fast muscle myosins, there are those isoforms that appear transiently during the course of muscle development. At a stage of development when two different myosins are coexpressed, the possibility arises for the existence of heterodimers, molecules containing two different heavy chains, or homodimers, molecules with two identical heavy chains. The question of whether neonatal and adult myosin isoforms can associate to form a stable heterodimer was addressed by using stage-specific monoclonal antibodies in conjunction with immunological and electron microscopic techniques. We find that independent of the ratio of adult to neonatal myosin, depending on the age of the animal, the myosin heavy chains form predominantly homodimeric molecules. The small amount of hybrid species present suggests that either the rod portion of the two heavy chain isoforms differs too much in sequence to form a stable alpha-helical coiled coil, or that the biosynthesis of the heavy chains precludes the formation of heterodimeric molecules.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.